Crystallization and preliminary diffraction analysis of a truncated homodimer of human phenylalanine hydroxylase

被引：17

作者：

Erlandsen, H

Martinez, A

Knappskog, PM

Haavik, J

Hough, E

Flatmark, T

机构：

[1] UNIV TROMSO, INST MATH & PHYS SCI, PROT CRYSTALLOG GRP, DEPT CHEM, N-9001 TROMSO, NORWAY

[2] UNIV BERGEN, DEPT BIOCHEM & MOL BIOL, BERGEN, NORWAY

[3] UNIV BERGEN, DEPT MED GENET, BERGEN, NORWAY

来源：

FEBS LETTERS | 1997年 / 406卷 / 1-2期

关键词：

phenylalanine hydroxylase; recombinant enzyme; truncated form; crystallization; X-ray diffraction analysis;

D O I：

10.1016/S0014-5793(97)00259-7

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A recombinant truncated form (Delta 1-102/Delta 428-452) of the non-heme iron-dependent metalloenzyme human phenylalanine hydroxylase (hPAH, phenylalanine 4-monooxygenase; EC 1.14.16.1) was expressed in E. coli, purified to homogeneity as a homodimer (70 kDa) and crystallized using the hanging drop vapour diffusion method, The crystals are orthorhombic, space group C222 with cell. dimensions of a=66.6 Angstrom, b=108.4 Angstrom, c=125.7 Angstrom. The calculated packing parameter (V-m) is 3.24 Angstrom(3)/Da with four 2-fold symmetric dimers (or eight momomers) in the unit cell, Data have been collected to 2.0 Angstrom resolution. (C) 1997 Federation of European Biochemical Societies.

引用

页码：171 / 174

页数：4

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